| Mutation | RNase Activity (nmol RNA/s/nmol RNase) | Fold Change vs. Wild-Type | Source |
|---|---|---|---|
| Wild-Type EDN | 4.2 | — | |
| Arg-132 → Thr (GZ-C) | 0.35 | 12× ↓ | |
| Ser-64 → Arg (GZ-F) | 0.057 | 74× ↓ | |
| Arg-64/Thr-132 → Ser/Arg | 13.0 | 15× ↑ |
The Thr-132→Arg substitution stabilizes substrate binding via electrostatic interactions with RNA phosphate groups .
Synergistic effects of Ser-64 and Arg-132 enhance catalytic efficiency by 13-fold in ancestral reconstructions .
Target Pathogen: Respiratory Syncytial Virus (RSV)
Binds extracellular RSV virions via N-terminal residues (34–38), promoting RNA degradation .
Antiviral activity is saturable and specific, unaffected by structurally unrelated RNases like RNase k6 .
| Protein | Infectious Units (% of Control) | Significance (p-value) | Source |
|---|---|---|---|
| Control Buffer | 100% | — | |
| Human EDN | 47% | <0.001 | |
| Owl Monkey EDN | 118% | NS | |
| Ancestral EDN (Node A) | 78% | <0.001 |
Evolutionary acquisition of antiviral activity occurred post-divergence of Old World (OW) and New World (NW) monkeys .
Gene Duplication: EDN diverged from ECP (~30 million years ago), gaining enhanced RNase activity through complementary substitutions .
Functional Divergence:
Therapeutic Potential:
Research Tools: